Investigate the Binding of Catechins to Trypsin Using Docking and Molecular Dynamics Simulation

	Investigate the Binding of Catechins to Trypsin Using Docking and Molecular Dynamics Simulation
	Cui,Fengchao; Yang,Kecheng; Li,Yunqi
刊名	plos one
	2015
卷号	10 期号:5 页码:5994-5998
关键词	DENSITY-FUNCTIONAL THERMOCHEMISTRY GREEN TEA POLYPHENOLS ALPHA-AMYLASE SERUM-ALBUMIN LUNG-CANCER FORCE-FIELD INHIBITORS PROTEIN EXCHANGE ENERGY
通讯作者	li,yq
英文摘要	to explore the inhibitory mechanism of catechins for digestive enzymes, we investigated the binding mode of catechins to a typical digestive enzyme-trypsin and analyzed the structure- activity relationship of catechins, using an integration of molecular docking, molecular dynamics simulation and binding free energy calculation. we found that catechins with different structures bound to a conservative pocket s1 of trypsin, which is comprised of residues 189-195, 214-220 and 225-228. in the trypsin-catechin complexes, asp189 by forming strong hydrogen bonding, and gln192, trp215 and gly216 through hydrophobic interactions, all significantly contribute to the binding of catechins. the number and the position of hydroxyl and aromatic groups, the structure of stereoisomers, and the orientation of catechins in the binding pocket s1 of trypsin all affect the binding affinity. the binding affinity is in the order of epigallocatechin gallate (egcg) > epicatechin gallate (ecg) > epicatechin (ec) > epigallocatechin (egc), and 2r-3r egcg shows the strongest binding affinity out of other stereoisomers. meanwhile, the synergic conformational changes of residues and catechins were also analyzed. these findings will be helpful in understanding the knowledge of interactions between catechins and trypsin and referable for the design of novel polyphenol based functional food and nutriceutical formulas.
收录类别	SCI
语种	英语
公开日期	2016-05-31
内容类型	期刊论文
源URL	[http://ir.ciac.jl.cn/handle/322003/67925]
专题	长春应用化学研究所_长春应用化学研究所知识产出_期刊论文
推荐引用方式 GB/T 7714	Cui,Fengchao,Yang,Kecheng,Li,Yunqi. Investigate the Binding of Catechins to Trypsin Using Docking and Molecular Dynamics Simulation[J]. plos one,2015,10(5):5994-5998.
APA	Cui,Fengchao,Yang,Kecheng,&Li,Yunqi.(2015).Investigate the Binding of Catechins to Trypsin Using Docking and Molecular Dynamics Simulation.plos one,10(5),5994-5998.
MLA	Cui,Fengchao,et al."Investigate the Binding of Catechins to Trypsin Using Docking and Molecular Dynamics Simulation".plos one 10.5(2015):5994-5998.